ID Q6FS05_CANGA Unreviewed; 1626 AA.
AC Q6FS05;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN OrderedLocusNames=CAGL0H04477g {ECO:0000313|CGD:CAL0132040,
GN ECO:0000313|EMBL:CAG59922.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59922.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59922.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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DR EMBL; CR380954; CAG59922.1; -; Genomic_DNA.
DR RefSeq; XP_446989.1; XM_446989.1.
DR STRING; 284593.Q6FS05; -.
DR EnsemblFungi; CAGL0H04477g-T; CAGL0H04477g-T-p1; CAGL0H04477g.
DR GeneID; 2888555; -.
DR KEGG; cgr:CAGL0H04477g; -.
DR CGD; CAL0132040; CAGL0H04477g.
DR VEuPathDB; FungiDB:CAGL0H04477g; -.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q6FS05; -.
DR OMA; GWFLWNI; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0070867; C:mating projection tip membrane; IEA:EnsemblFungi.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IEA:EnsemblFungi.
DR GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140345; F:phosphatidylcholine flippase activity; IEA:EnsemblFungi.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:EnsemblFungi.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IEA:EnsemblFungi.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 2.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR24092:SF174; PHOSPHOLIPID-TRANSPORTING ATPASE DNF3-RELATED; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1306..1329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1341..1358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1370..1394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1414..1434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 121..176
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 1196..1444
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 835..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1626 AA; 185199 MW; 6132FF6543B9ACB8 CRC64;
MTEPDKKRKR SWSLRTQMFN KHLFENYHND DNVEMNDIDE ETENDEGHIG DFNSIDGQTK
IRNHQSPRLV TKILDMLFDR RTQVHSVDGR HIPISLDHSS AISDIYPVDR HGNLVDERYG
YAYCNNLITS SRYTIISFFP RQLYAQFSKL ANVYFFIVAI LQMIPGWSTT GTYTTIVPLC
VFMAISMARE AYDDYRRHKL DKEENNKLTK VLQILHERED NDLDLENNAQ HSANNPESIS
NLYFNNFDLL AKKYNVRIVE KKWKDIRVGD FVLLQQDDWV PADILILTSD GDNSEVFIET
MALDGETNLK GKVPHPEINK LTKSASGLAN INAQVTVEDP NNDLYNFEGN LELNSGSSSK
KKYPLGPDNV IYRGSIIRNT RNCVGMVIFT GEESKIRMNA LRNPRTKAPK LQRKINMIVV
FMVFVVACMS LFSYLGHTIQ IKRYVNNNKA WYLLQEDAGT APTIMSFIIM YNTIIPLSLY
VTMELIKVAQ SRMMEWDIDM YHAESDTPCA VRTATILEEL GQVSYIFSDK TGTLTDNKML
FRKLSFCGTS WVHNATQDIS EFKPAQLSNK NDIDVISIDD QSFLSKLGYT SQSNPKRYMD
INDFPDRRTS VEYKGNATVK YTGRPSMRSL YVPPKKETNA SNSQDASDIP EDIKSTFELI
YYIQSNPKSL FAKKAKMFIL SLAICHICLP KRTEEGNDED DIIEYQSSSP DELALVTAAR
DMGYIVYNRN ANILTLKTFP DGFDELPRFE NFEILELVDF NSQRKRMSVI VRVPEEKDRV
LLFCKGADNV ILERLHNKEM ALDMLDQVEN NTKYRKDAEA ELVIQHRKSL ERAVNDDLPR
TSLRNSISRG PRESLSLQAA RKSMSRKSNQ LQDPEMQLGT IDQFLDSVQK TDKEIDAVVS
QARKSLAKQR LEKYGPRLSM DSPQIVAAEK SPQVSNGNDV LLNYIGSDAL ISNEEYVLEK
TLEDIESFST EGLRTLLFAH KWISNEDFEQ WRTRYHEAKT SLSERKQKID EVGAQIEDEL
YLLGATAIED KLQEGVSEAI EKIRRAGIKM WMLTGDKRET AINIGYSCKL IHDYSTVVIL
TTSDENIISK MNAISQEVDS GNVAHCVIVI DGATLAMFED NPTLMSVFTE LCTKTDSVVC
CRASPAQKAL MVSNIRNTDK SIVTLAIGDG ANDIAMIQSA DIGVGIAGKE GLQASRSADY
SIGQFRFILK LLLVHGRYNY IRTAKFILCT FYKELTFYLT QLIYQRYTMF SGTSLYEPWS
LSMYNTLFTS LPVLCVGMFE KDLKPVTLLT VPELYSMGRL SKAFNWSIFA EWVFLGTANA
LIITFLNIVA WGETSLSDNT LYPLGFVNFS ATVALINVKA QFIEMRNRNW LAFTSVILSC
GGWLVWCCAL PILNRSDGIY DVTYGLYHHF GRDITFWCTS LILAVLPIIV DVVYKTFKIM
LAPSDSDIFA ELEQKSEIRK KLELGAYNEM KQGWTWTQDQ STFDKYKDIV FNRSRSASSA
TEVNSMTNLA HGNSEDDQYL SSRFANDDIH TSYSGNSATS PPKPTRGNSL KLLSLNITGN
SRSSEEYEVL PSGKLIKRQS TELQKATNNS ENMASKLTKK LRFKMKDEED DEEIDRIIRD
RMKDLE
//
